1mpj | pdb_00001mpj

X-RAY CRYSTALLOGRAPHIC STUDIES ON HEXAMERIC INSULINS IN THE PRESENCE OF HELIX-STABILIZING AGENTS, THIOCYANATE, METHYLPARABEN AND PHENOL

spinqualitylabelsall models 1mpj, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1mpj is a 4 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: CL, IPH, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function INS_PIG Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Three X-ray crystallographic studies have been carried out on pig insulin in the presence of three ligands, thiocyanate, methylparaben (methyl p-hydroxybenzoate), and phenol. In each case, rhombohedral crystals were obtained, which diffracted to 1.8, 1.9, and 2.3 A, respectively. Each crystal structure was very similar to that of 4-zinc pig insulin, which was used as a starting model for PROLSQ refinement (Collaborative Computational Project, Number 4, 1994). The R factors for the refined structures of thiocyanate insulin, methylparaben insulin, and phenol insulin were 19.6, 18.4, and 19.1, respectively. Each crystal structure consists of T3R3f insulin hexamers with two zinc ions per hexamer. In the R3f trimer of the thiocyanate insulin hexamer, one thiocyanate ion is coordinated to the zinc on the hexamer 3-fold axis, but there is no evidence of zinc ion binding in the off-axis zinc ion sites seen in the 4-zinc pig insulin structure. In the methylparaben insulin and phenol insulin hexamers, the phenolic ligands are bound at the dimer-dimer interfaces in the R3f trimers in a manner similar to that of phenol in R6 phenol insulin. The binding of methylparaben appears to make the hexamer more compact by drawing the A and the B chains closer together in the binding site. In all three structures presented herein, the conformations of the first three residues of the B chain in the R3f trimer are extended rather than alpha-helical, as is seen in R6 phenol insulin. The energetics of ligand binding in the insulin hexamer are discussed. X-ray crystallographic studies on hexameric insulins in the presence of helix-stabilizing agents, thiocyanate, methylparaben, and phenol.,Whittingham JL, Chaudhuri S, Dodson EJ, Moody PC, Dodson GG Biochemistry. 1995 Nov 28;34(47):15553-63. PMID:7492558 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Insulin 3D Structures

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